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Aurora A Regulates the Activity of HURP by Controlling the Accessibility of Its Microtubule-Binding Domain.

Authors
Jim WongRobert LerrigoJang, Chang YoungGuowei Fang
Issue Date
May-2008
Publisher
AMER COC CELL BIOLOGY
Citation
Molecular Biology of The Cell, v.19, no.5, pp 2083 - 2091
Pages
9
Journal Title
Molecular Biology of The Cell
Volume
19
Number
5
Start Page
2083
End Page
2091
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/151502
DOI
10.1091/mbc.E07-10-1088
ISSN
1059-1524
Abstract
HURP is a spindle-associated protein that mediates Ran-GTP-dependent assembly of the bipolar spindle and promotes chromosome congression and interkinetochore tension during mitosis. We report here a biochemical mechanism of HURP regulation by Aurora A, a key mitotic kinase that controls the assembly and function of the spindle. We found that HURP binds to microtubules through its N-terminal domain that hyperstabilizes spindle microtubules. Ectopic expression of this domain generates defects in spindle morphology and function that reduce the level of tension across sister kinetochores and activate the spindle checkpoint. Interestingly, the microtubule binding activity of this N-terminal domain is regulated by the C-terminal region of HURP: in its hypophosphorylated state, C-terminal HURP associates with the microtubule-binding domain, abrogating its affinity for microtubules. However, when the C-terminal domain is phosphorylated by Aurora A, it no longer binds to N-terminal HURP, thereby releasing the inhibition on its microtubule binding and stabilizing activity. In fact, ectopic expression of this C-terminal domain depletes endogenous HURP from the mitotic spindle in HeLa cells in trans, suggesting the physiological importance for this mode of regulation. We concluded that phosphorylation of HURP by Aurora A provides a regulatory mechanism for the control of spindle assembly and function.
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